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OL56_STRAT
ID   OL56_STRAT              Reviewed;        3519 AA.
AC   Q07017;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Oleandomycin polyketide synthase, modules 5 and 6;
GN   Name=orfB;
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8107683; DOI=10.1007/bf00280426;
RA   Swan D.G., Rodriguez A.M., Vilches C., Mendez C., Salas J.A.;
RT   "Characterisation of a Streptomyces antibioticus gene encoding a type I
RT   polyketide synthase which has an unusual coding sequence.";
RL   Mol. Gen. Genet. 242:358-362(1994).
CC   -!- FUNCTION: May be involved in the biosynthesis of the oleandomycin
CC       lactone ring.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC       Note=Binds 2 phosphopantetheines covalently.;
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DR   EMBL; L09654; AAA19695.1; -; Unassigned_DNA.
DR   PIR; S43048; S43048.
DR   SMR; Q07017; -.
DR   ESTHER; strat-ol56; Thioesterase.
DR   PRIDE; Q07017; -.
DR   KEGG; ag:AAA19695; -.
DR   BioCyc; MetaCyc:MON-17052; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 2.
DR   Gene3D; 3.40.366.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR041618; PKS_DE.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR036299; Polyketide_synth_docking_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 2.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 2.
DR   Pfam; PF18369; PKS_DE; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 2.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF101173; SSF101173; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 4.
DR   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   SUPFAM; SSF55048; SSF55048; 2.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Acyltransferase; Antibiotic biosynthesis; Multifunctional enzyme; NADP;
KW   Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT   CHAIN           1..3519
FT                   /note="Oleandomycin polyketide synthase, modules 5 and 6"
FT                   /id="PRO_0000180297"
FT   DOMAIN          1489..1564
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3143..3218
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          1..?
FT                   /note="Module 5"
FT   REGION          32..501
FT                   /note="Beta-ketoacyl synthase 1"
FT   REGION          569..890
FT                   /note="Acyltransferase (AT) 1"
FT   REGION          1200..1382
FT                   /note="Beta-ketoacyl reductase 1"
FT   REGION          1686..2156
FT                   /note="Beta-ketoacyl synthase 2"
FT   REGION          2220..2541
FT                   /note="Acyltransferase (AT) 2"
FT   REGION          2856..3038
FT                   /note="Beta-ketoacyl reductase 2"
FT   REGION          3224..3245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3270..3519
FT                   /note="Thioesterase"
FT   REGION          ?..3519
FT                   /note="Module 6"
FT   ACT_SITE        210
FT                   /note="For beta-ketoacyl synthase 1 activity"
FT   ACT_SITE        660
FT                   /note="Acyl-ester intermediate"
FT   ACT_SITE        1859
FT                   /note="For beta-ketoacyl synthase 2 activity"
FT   ACT_SITE        2311
FT                   /note="Acyl-ester intermediate"
FT   BINDING         1203..1249
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         2859..2905
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   MOD_RES         1524
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3178
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3519 AA;  368567 MW;  41AE78AAAEB61F86 CRC64;
     MAEAEKLREY LWRATTELKE VSDRLRETEE RAREPIAIVG MSCRFPGGGD ATVNTPEQFW
     DLLNSGGDGI AGLPEDRGWD LGRLYDPDPD RAGTSYVREG GFLYDSGEFD AAFFGISPRE
     ALAMDPQQRL LLETSWEAFE SAGIKRAALR GSDTGVYIGA WSTGYAGSPY RLVEGLEGQL
     AIGTTLGAAS GRVAYTFGLE GPAVTVDTAC SSSLVALHLA VQGLRRGECS LALVGGVTVM
     SSPVTLTTFS RQRGLSVDGR CKAFPASADG FGAAEGVGVL LVERLSDARR LGHRVLAVVR
     GSAVNQDGAS NGLTAPNGPS QQRVIRAALA DAGLAPADVD VVEAHGTGTR LGDPIEAQAL
     LATYGQGRAG GRPVWLGSVK SNIGHTQAAA GVAGVMKMVL ALGRGVVPKT LHVDEPSPHV
     DWSAGAVELL TEERPWEPEA ERLRRAGISA FGVSGTNAHV IVEEAPAEPE PEPGTRVVAA
     GDLVVPWVVS GRDARALRAQ AARLAAHVSG VSAVDVGWSL VATRSVFEHR AVAIGSELDS
     MAGSLAGFAA GGVVPGVVSG VAPAEGRRVV FVFPGQGSQW VGMAAGLLDA CPVFAEAVAE
     CAAVLDPVTG WSLVEVLQGR DATVLGRVDV VQPALWAVMV SLARTWRYYG VEPAAVVGHS
     QGEIAAACVA GGLSLADGAR VVVLRSRAIA RIAGGGGMVS VSLPAGRVRT MLEEFDGRLS
     VAAVNGPSST VVSGDVQALD ELLAGCEREG VRARRVPVDY ASHSAQMDQL RDELLEALAD
     ITPQDSSVPF FSTVTADWLG TTALGAGYWF TNLRETVRFQ EAVEGLVAQG MGAFVECSPH
     PVLVPGIEQT LDALDQNAAV FGSLRRDEGG LDRFLTSLAE AFVQGVPVDW SRAFEGVTPR
     TVDLPTYPFQ RQHYWLMAEE APVSQPPHSE NSFWSVVADA DAEAAAELLG VDVEAVEAVM
     PALSSWHRQS QLRAEVNQWR YDVAWKRLTT GALPEKPGNW LVVTPAGTDT TFAESLARTA
     AAELGVSVSF AQVDTAHPDR SQYAHALRQA LTGPENVDHL VSLLALDQAT DDLAAAPSCL
     AASLVLAQAL VDLGRVGEGP RLWLVTRGAV VAGPSDAGAV IDPVQAQVWG FGRVLGLEHP
     ELWGGLIDLP VGVDEEVCRR FVGVVASAGF EDQVAVRGSG VWVRRLVRAV VDGGGGGWRP
     RGTVLVTGGL GGLGAHTARW LVGGGADHVV LVSRRGGSAP GAGDLVRELE GLGGARVSVR
     ACDVADRVAL RALLSDLGEP VTAVFHAAGV PQSTPLAEIS VQEAADVMAA KVAGAVNLGE
     LVDPCGLEAF VLFSSNAGVW GSGGQAVYAA ANAFLDALAV RRRGVGLPAT SVAWGMWAGE
     GMASVGGAAR ELSRRGVRAM DPERAVAVMA DAVGRGEAFV AVADVDWERF VTGFASARPR
     PLISDLPEVR AVVEGQVQGR GQGLGLVGEE ESSGWLKRLS GLSRVRQEEE LVELVRAQAA
     VVLGHGSAQD VPAERAFKEL GFDSLTAVEL RNGLAAATGI RLPATMAFDH PNATAIARFL
     QSQLLPDAES ESAVPSSPED EVRQALASLS LDQLKGAGLL DPLLALTRLR EINSTVQNPE
     PTTESIDEMD GETCCAWRSA KSTAEPLTTG ADMPDPTAKY VEALRASLKE NERLRQQNHS
     LLAASREAIA ITAMSCRFGG GIDSPEDLWR FLAEGRDAVA GLPEDRGWDL DALYHPDPEN
     PGTTYVREGA FRYDAAQFDA GFFGISPREA LAMDPQQRLL LETSWELFER ADIDPYTVRG
     TATGIFIGAG HQGYGPDPKR APESVAGYLL TGTASAVLSG RISYTFGLEG PAVTVDTACS
     SSLVALHLAV QALRRGECSL AIAGGVAVMS TPDAFVEFSR QQGMARDGRC KAFAAAADGM
     GWGEGVSLLL LERLSDARRL GHRVLAVVRG SAVNQDGASN GLAAPNGPSQ QRVIRAALAD
     AGLAPADVDV VEAHGTGTRL GDPIEAQALL ATYGQGRAGG RPVWLGSVKS NIGHTQAAAG
     VAGVMKMVLA LGRGVVPKTL HVDEPSPHVD WSAGAVELLT EERPWEPEAE RLRRAGISAF
     GVSGTNAHVI VEEAPAEPEP EPGTRVVAAG DLVVPWVVSG RDVGALREQA ARLAAHVSST
     GAGVVDVGWS LVATRSVFEH RAVMVGTDLD SMAGSLAGFA AGGVVPGVVS GVAPAEGRRV
     VFVFPGQGSQ WVGMAAGLLD ACPVFAEAVA ECAAVLDPVT GWSLVEVLQG RDATVLGRVD
     VVQPALWAVM VSLARTWRYY GVEPAAVVGH SQGEIAAACV AGGLSLADGA RVVVLRSRAI
     ARIAGGGGMV SVSLPAGRVR TMLDTYGGRV SVAAVNGPSS TVVSGDVQAL DELLAGCERE
     GVRARRVPVD YASHSAQMDQ LRDELLEALA DITPQDSSVP FFSTVTADWL DTTALDAGYW
     FTNLRETVRF QEAVEGLVAQ GMGAFVECSP HPVLVPGIEQ TLDALDQNAA VLGSLRRDEG
     GLDRLLTSLA EAFVQGVPVD WTHAFEGVTP RTVDLPTYPF QRQRFWLDGS PASSANGVDG
     EADAMIWDAV EREDSVAVAE ELGIDAEALH TVLPALSSWR RRRVEHRRLQ DWRYRVEWKP
     FPAALDEVLG GGWLFVVPRG LADDGVVARV VAAVTARGGE VSVVELDPTR PDRRAYAEAV
     AGRGVSGVVS FLSWDDRRHS EHPVVPAGLA ASLVLAQALV DLGRVGEGPR LWLVTRDAVV
     AGPSDAGAVI DPVQAQVWGF GRVLGLEHPE LWGGLIDLPV EAPEPGSTCD HTYADLLATV
     VASAGFEDQV AVRGSGVWVR RLVRAVVDGG GGGWRPRGTV LVTGGLGGLG AHTARWLVGG
     GADHVVLVSR RGGSAPGAGD LVRELEGLGG ARVSVRACDV ADRVALRALL SDLGEPVTAV
     FHAAGVPQST PLAEISVQEA ADVMAAKVAG AVNLGELVDP CGLEAFVLFS SNAGVWGSGG
     QAVYAAANAF LDALAVRRRG VGLPATSVAW GMWAGEGMAS VGGAARELSR RGVRAMDPER
     AVAVMADAVG RGEAFVAVAD VDWERFVTGF ASARPRPLIS DLPEVRTALR NQEQEQLHAP
     VPEDRSAQLL RRLSMLSPAG REAELVKLVR TEAAAVLGHG SAQDVPAERA FKELGFDSLT
     AVQLRNRLAA ATGTRLPASA VFDHPHAAAL ARWLLAGMRH ADGGHGGGHA GGPGPDADEG
     RSAGAGHSGM LADLYRRSAE LGRSREFIGL LADTAAFRPV FHGPADLDAP LEAVPLADGV
     RKPQLICCSG TAPVGGPHEF ARLASFFRGT RAVSALPLPG YLPGEQLPAD LDAVLAAQAE
     AVEKQTGGAP FVLVGYSAGG LMAHALACHL AGRGTPPSGE VLVDVYPPGR QEPVFGWQKE
     LTEGMFAQDF VPMDDTRLTA LGTYDRLMGE WRPAPSGLPT LLIRATEPMA EWTGAIDWRA
     SWEYDHTAVD MPGNHFTIMR EHAEDAARHI DVWLKGLTP
 
 
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